Angiotensin converting enzyme is an important structural enzyme in the lung which hydrolyzes angiotensin 1 to vasoactive angiotensin 2 and inactivates bradykinin by its dipeptidyl hydrolase activity. We have purified and studied this enzyme from rat lung and guinea pig lung and serum and human serum. We plan to continue studies on the purification of this enzyme from various sources and on its physical, biochemical, and immunological properties. In particular, we wish to study the relationship of this enzyme in the lung to that in blood and in other tissues. We plan to obtain information about its localization in tissue by immunologic techniques and in particular to study its biological role in sarcoidosis where it is elevated in serum. We hope to gain information about its site of synthesis and possible mode of release from the cell with the use of in vitro techniques and to determine if pulmonary disease processes result in alterations in converting enzyme in the lung or in the systemic circulation. We plan to extend these studies in a similar manner to other enzymes in the pulmonary circulation, including lipoprotein lipase, prostaglandin dehydrogenase, nucleotidase, and nucleoside and nucleotide deaminase, which may play important roles at the alveolar capillary interface. BIBLIOGRAPHIC REFERENCES: Lanzillo, J. J. and B. L. Fanburg. Angiotensin I converting enzyme from guinea pig lung and serum: A comparison of some kinetic and inhibition properties. Biochim. Biophys. Acta 445:161, 1976. Lanzillo, J. J. and B. L. Fanburg. Low molecular weight angiotensin 1 converting enzyme from rat lung. Biochim. Biophys. Acta 491: 339, 1977.